I want to study which arginine or lysine residues in target proteins are preferentially modified by glycating agents like methylglyoxal. Is there a database or any other resource which lists the modified proteins with specific data on the amino acid position and the nature of the modification (e. g., MG-H1 at position Arg xy in protein z)?
I would appreciate your help.
Thanks and best regards, Christian
Dear Christian,
I couldn't find a database of glycated proteins. But I found some databases which might be useful for your work.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. http://www.ebi.ac.uk/interpro/
GlycoSiteAlign selectively aligns amino acid sequences surrounding glycosylation sites (by default, 20 positions on each side of the glycosylated residue) depending on structural properties of the glycan attached to the site. http://glycoproteome.expasy.org/glycositealign/
NetGlycate 1.0 server predicts glycation of ε amino groups of lysines in mammalian proteins. http://www.cbs.dtu.dk/services/NetGlycate/
The NetOglyc server produces neural network predictions of mucin type GalNAc O-glycosylation sites in mammalian proteins. http://www.cbs.dtu.dk/services/NetOGlyc/
The NetNglyc server predicts N-Glycosylation sites in human proteins using artificial neural networks that examine the sequence context of Asn-Xaa-Ser/Thr sequons. http://www.cbs.dtu.dk/services/NetNGlyc/
Thanks a lot, Arman! Especially the NetGlycate server is very useful for me.
Cheers, Christian
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